A study of the kinetics and properties of immobilized glycosidases will be developed toward their potential use in the treatment of hereditary glycosidic enzyme deficiency diseases. The immobolized glycosidases are reusable, more stable than in their soluble state and in a form that makes them ideal delivery vehicles in enzyme replacement therapy by either direct implantation or extracorporeal perfusion. The initial studies will include Beta-N-acetylgalactosaminidase, Beta-N-acetylgalactosaminidase, Alpha Beta-galactosidase, Beta-glucosidase, and later expanded to include Alpha-fucosidase, Alpha-mannosidase and Alpha-mannosidase and Alpha-N-acetylglucosaminidase. The properties and kinetic characteristics of the glycolipid glycosyl transferases involved in brain ganglioside biosynthesis will be further investigated. The conditions for reversibility of some of these transferases will be determined so that a new strategy for a therapeutic approach in degrading an accumulaaed glycolipid in a glycolipid storage disease could be formulated.